Dr. Shannon Servoss

 Dr. Shannon Servoss

Development of biomimetic materials based on poly-N-substituted glycine (peptoid) constructs for use in biomedical applications

1.   Peptoids are easy and inexpensive to synthesize using an automatic peptide synthesizer, and can be designed to form extremely stable secondary structures.  In addition, previous studies have shown that properly designed peptoids create a robust surface coating that resists the attachment of proteins and cellular debris.  These structures take on various forms, such as micropores and microspheres, depending on side chain chemistry and the solvent.  A coating that incorporates the various attributes of peptoids would be ideal for microarrays, as it would (i) allow for increased surface area for antibody immobilization, (ii) create a barrier between the glass slide and the antibody to retain function, (iii) be easy and inexpensive to synthesize, and (iv) minimize the background signal due to non-specific protein binding.  Peptoids are also ideal candidates for use as an affinity reagent due to their inexpensive and facile synthesis, ability to incorporate unique reactive sites, highly stable helical structures, and potential for non-biofouling design.  A peptoid designed for stability and with included reactive sites will serve as the support for an affinity reagent, essentially mimicking the constant region of an antibody.  Reactive sites on the surface of the peptoid will be used to incorporate antigen binding peptides/peptoids.  

2.   While researchers are discovering many potential biomarkers for early stage cancer, validating these biomarkers for use in diagnostic systems is becoming increasingly difficult.  The standard technique for validation is enzyme-linked immunosorbent assay, which requires two good affinity reagents against the biomarker.  There are a limited number of affinity reagents currently available and the techniques for affinity reagent development are slow and expensive, greatly limiting the validation of biomarkers.  Synthetic affinity reagents, such as affitoids, have the potential to be screened for much more rapidly than is currently possible.  The rapid discovery of affinity reagents will ultimately lead to rapid validation of early stage breast cancer biomarkers, and thus a quicker path to a clinical diagnostic for early stage breast cancer.

 

 Dr. C Hestekin

Dr. Christa Hestekin

Investigation of early stage protein aggregation using microchannel electrophoresis

Early stage protein aggregation has been implicated in a variety of diseases in includeing alzheimer's disease and diabetes. Alzheimer's Disease (AD) is a complex and devastating neurodegenerative disease.  Currently, AD is believed to progress from harmless amyloid beta (Aβ) monomers through a nucleation step to oligomeric species and then larger aggregates.  There is a need to develop a technique that can detect the aggregation of early species (oligomers) at physiological concentrations with rapid analysis times.  Microchannel electrophoresis offers an attractive approach for detecting low concentration, transient species that may be key to the development of Alzheimer’s disease.  The Hestekin lab has previously explored the use of microchannel electrophoresis to investigate the effects of solution conditions and sample preparation on the oligomeric, pre-beta sheet aggregates.  The lab is currently focused on investigating changes to the primary sequence that alter the protein’s aggregation in an effort to understand the driving mechanism.  The information gleaned from these studies could be used to enhance drug design.  In addition, the conditions for physiological detection of protein aggregates using fluorescent labels as well as the separation and identification of individual oligomeric species are also being explored

 

 


 

Dr. Bob Beitle

 

Dr. Bob Beitle

Biochemical engineering, with an emphasis on bioseparation and fermentation, and adaptive technology for the disabled

 

 

 

 

 

 

 

 

 

 

 

 

Dr. Donald Roper

 

Dr. Donald K. Roper

      Dr. Roper examines electrodynamics in nanomaterials and bio/chemical systems for biomedicine, sustainable energy, and optoelectronics.  Particular examples are light-active nanostructured metamaterials (e.g., nanoplamonics) for detectors, microarrays, and NEMS; nanolithography and electron microscopy for sensors, optodes, and sensorimotor circuits; graphene and stanene-based 2D materials.  Dr. Roper has developed processes for cell culture, fermentation, biorecovery and analysis of polysaccharide, protein, DNA and adenoviral-vectored antigens at Merck & Co. (West Point, PA), extraction of photodynamic cancer therapeutics at Frontier Scientific, Inc. (Logan, UT), and virus binding methods for Millipore Corp (Billerica, MA).